Substrate selectivity of artificial transaminase constituted with functionalized bilayer membrane.
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概要
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The transamination reactions of α-amino acid derivatives with α-keto acids as catalyzed by an artificial transaminase were examined in aqueous media under mild conditions. The present artificial holoenzyme was constituted with a combination of a cationic peptide lipid having a L-histidyl residue, a hydrophobic pyridoxamine derivative, and copper(II) ions, and found to exercise marked substrate selectivity which came from the molecular recognition in the course of formation of the aldimine Schiff-base chelates composed of the hydrophobic pyridoxal derivative, α-amino acids, and copper(II) ions. The transamination reaction of the hydrophobic β-benzyl L-aspartate with the hydrophilic pyruvate was most effectively catalyzed among 18 combinations of substrate species employed here. Enantioselectivity was observed for the catalytic transamination of phenylalanine with pyruvate.
- 公益社団法人 日本化学会の論文
著者
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Murakami Yukito
Department Of Chemical Science And Technology Faculty Of Engineering Kyushu University
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KIKUCHI Jun-ichi
Department of Applied Chemistry, Faculty of Science and Engineering, Saga University
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Kikuchi Jun-ichi
Department of Organic Synthesis, Faculty of Engineering, Kyushu University
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Shiratori Nobuyuki
Department of Organic Synthesis, Faculty of Engineering, Kyushu University
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